Dataset Information

Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation

ABSTRACT: DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-forming CTPase ParB. The lifetime of these interactions is limited by the ParB-dependent activation of ParA ATPase activity. Here, we elucidate the functional interplay between ParA and ParB in the model bacterium Myxococcus xanthus. We demonstrate that the N-terminal ParA-binding motif of ParB associates with a conserved bipartite binding pocket at the ParA dimer interface, in a manner dependent on ParB clamp closure. Moreover, we show that ParB and non-specific DNA interact cooperatively with ParA and synergistically induce structural changes at its Walker A and Walker B motifs that correlate with the activation of ParA ATPase activity. These results advance our understanding of the mechanism underlying DNA transport by the ParABS system and may help to unravel the mode of action of related cargo-positioning systems.

INSTRUMENT(S):

ORGANISM(S): Myxococcus Xanthus Dk 1622

SUBMITTER: Wieland Steinchen

LAB HEAD: Gert Bange

PROVIDER: PXD063735 | Pride | 2025-08-11

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Dataset1_220214_HX_097_Tb.DnX	Other
	Dataset1_220214_HX_097_Tb_PLGS.zip	Other
	Dataset1_220214_HX_097_Tb_State1.zip	Other
	Dataset1_220214_HX_097_Tb_State2.zip	Other
	Dataset1_220214_HX_097_Tb_State3.zip	Other

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Publications

Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.

Schnabel Lucas L Osorio-Valeriano Manuel M Perez-Borrajero Cecilia C Steinchen Wieland W Mais Christopher-Nils CN Simon Bernd B Hanßmann Juri J Thamm Maria M Hennig Janosch J Bange Gert G Thanbichler Martin M

Nature communications 20250925 1

DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-forming CTPase ParB. The lifetime of these interactions is limited by the ParB-dependent activation of ParA ATPase activity. Here, we elucidate the functional interplay between ParA and ParB in the model bacterium Myxococcus xanthus. We demonstrate that the N-terminal ParA-binding motif of ParB associa ...[more]

PMID: 40998818

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